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Histone H3 is a nuclear protein and a component of the nucleosome core, a basic unit of chromatin, that is essential for organizing genomic DNA in eukaryotic nuclei.1 It is a globular protein that contains an unstructured N-terminal tail that extends outside of the nucleosome core and is subject to various post-translational modifications (PTMs), including methylation, phosphorylation, acetylation, and citrullination.1,2 Dimethylation of histone H3 at lysine 79 (H3K79Me2) is a cell cycle-dependent modification associated with gene repression that is low during G1 and early S phases, increases during late S phase, and is maintained during G2/M.3 Levels of H3K79Me2 are increased during mitosis in a histone H2B monoubiquitination-dependent manner, and loss of H3K79Me2 is associated with increased chromosome numbers and mitotic defects in HCT116 cells.4 H3K79Me2 is completely absent in postmortem brain tissue isolated from fetuses with spina bifida.5 Cayman’s Histone H3K79Me2 Monoclonal Antibody (RM181) can be used for chromatin immunoprecipitation (ChIP), ELISA, immunohistochemistry (IHC), multiplex-based assay, and Western blot (WB) applications.
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1. Writing, erasing and reading histone lysine methylations. Exp. Mol. Med. 49(4), e324 (2017).
2. Histone posttranslational modifications: Potential role in diagnosis, prognosis, and therapeutics of cancer. Prognostic Epigenetics 15, 351-373 (2019).
3. Linking the cell cycle to histone modifications: Dot1, G1/S, and cycling K79me2. Mol. Cell. 35(6), 729-730 (2009).
4. Mitotic accumulation of dimethylated lysine 79 of histone H3 is important for maintaining genome integrity during mitosis in human cells. Genetics 199(2), 423-433 (2015).
5. Histone modification mapping in human brain reveals aberrant expression of histone H3 lysine 79 dimethylation in neural tube defects. Neurobiol. Dis. 54, 404-413 (2013).